Recombinant Human Antibody (hu5B3.v3) is capable of binding to HCV E2, expressed in HEK 293 cells. Expressed as the combination of a heavy chain (HC) containing VH from anti-HCV E2 mAb and CH1-3 region of human IgG and a light chain (LC) encoding VL from anti-HCV E2 proteins mAb and CL of human kappa light chain. Exists as a disulfide linked dimer of the HC and LC hetero-dimer under non-reducing condition. These data suggest that both MRCT10. v362 and hu5B3.v3 bind similar epitopes through different interactions.
Figure 1 HCVpp neutralization of affinity-matured E2⁴¹²⁻⁴³²-specific antibodies
Pantua, H., Diao, J., Ultsch, M., Hazen, M., Mathieu, M., McCutcheon, K., ... & Hass, P. (2013). Glycan shifting on hepatitis C virus (HCV) E2 glycoprotein is a mechanism for escape from broadly neutralizing antibodies. Journal of molecular biology, 425(11), 1899-1914.
Figure 2 Identification and characterization of mutant Jc1 and Con1/C3-neo HCVcc resistant to E2412–423-specific neutralizing antibody (AP33).
(a) Supernatants and cells from Jc1 (squares) and Con1/C3-neo (circles) HCVcc-infected Huh7.5 cells were sequentially cultured in the absence (filled symbols) or presence (open symbols) of increasing concentrations of AP33, and (b) HCV RNA replication was measured at various times post infection. These are representative data from three independent experiments. (c) 454 Ultra deep sequencing analysis of N417 amino acid variations over time demonstrating an enrichment of the N417S mutant HCVcc when cultured in the presence of antibody (WT, black; N417S, red; N417T, orange; N417G, green). (d) The effect of the mutations on HCVcc infectivity was determined by introducing them in Jc1 HCVcc and monitoring growth in culture over 9 days. (e and f) The effect of the identified mutations on infectivity of HCVpp was determined. HCVpp stocks were generated and normalized using p24 levels in the supernatants (e) followed by infecting Huh7.5 cells to measure infectivity (f). No pseudoparticles were generated in the absence of E1E2-expressing plasmid as determined by p24 levels. In vitro growth and infectivity studies are representative data from at least two independent experiments. p values: *p < 0.05, **p < 0.01 and ***p < 0.001.
Pantua, H., Diao, J., Ultsch, M., Hazen, M., Mathieu, M., McCutcheon, K., ... & Hass, P. (2013). Glycan shifting on hepatitis C virus (HCV) E2 glycoprotein is a mechanism for escape from broadly neutralizing antibodies. Journal of molecular biology, 425(11), 1899-1914.
Figure 3 Binding of hu5B3.v3 and MRCT10.v362 to wild-type and mutant soluble E2 proteins (sE2661) and E2412–423 peptides.
(a) Ratio of dissociation constants (KD) for MRCT10.v362 (red) and hu5B3.v3 (black) binding to alanine mutant peptides relative to WT peptide QLINTNGSWHINGSGK-biotin (E2⁴¹²⁻⁴³²-biotin) are graphed. Asterisks denote no binding detected with mutant peptides. (b) Binding of various E2⁴¹²⁻⁴³²-specific neutralizing antibodies to lysates of untransfected 293 cells (No E2) or 293 cells transfected with genotype 2a (J6CF) HCV E1E2-expressing plasmids containing various mutations at N415 or N417. These are representative data from three independent experiments. (c and d) MRCT10 Fab binds to N417S E2⁴¹²⁻⁴³². Biacore sensorgrams demonstrating binding of MRCT10 Fab to WT (c) or N417S (d) E2⁴¹²⁻⁴³² peptide. The Fab series was diluted 2-fold starting from 1000 nM down to 15.6 nM. MRCT10 Fab binds to N417S E2⁴¹²⁻⁴³² peptide with faster off-rate compared to WT. Dissociation constants (KD) are listed in the graphs.
Pantua, H., Diao, J., Ultsch, M., Hazen, M., Mathieu, M., McCutcheon, K., ... & Hass, P. (2013). Glycan shifting on hepatitis C virus (HCV) E2 glycoprotein is a mechanism for escape from broadly neutralizing antibodies. Journal of molecular biology, 425(11), 1899-1914.
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CAT | Product Name | Application | Type |
---|---|---|---|
PABL-040 | Recombinant Mouse Anti-CHIKV E2 glycoprotein Antibody (5F-10) | IF, Neut, IP | IgG |
PABL-118 | Recombinant Rat Anti-HCV E2 Antibody (3/11) | WB, ELISA, Neut, FuncS | IgG |
PABL-357 | Recombinant Human Anti-VEEV E2 Antibody (F5) | WB, ELISA, Neut, FuncS | IgG |
PABZ-180 | Recombinant Mouse Anti-HCV E2 Antibody (mAb#8) | Neut | IgG |
PABC-184 | Recombinant Chimeric (Human/Mouse) Anti-HCV glycoprotein E2 Antibody (mAb1:7) | Neut | IgG |
CAT | Product Name | Application | Type |
---|---|---|---|
PSBL-357 | Recombinant Human Anti-VEEV E2 Antibody scFv Fragment (F5) | WB, ELISA, Neut, FuncS | scFv |
PSBL-462 | Recombinant Mouse Anti-Epitope II of HCV E2 Antibody scFv Fragment (mAb 12) | WB, FuncS | scFv |
PSBL-502 | Recombinant Rat Anti-HCV E2 antigenic region 412-423 Antibody scFv Fragment (311) | Neut | scFv |
HPAB-N0072-YC-S(P) | Recombinant Human Anti-E2 Antibody scFv Fragment (HC84.26.5D) | Neut, ELISA, FuncS | Human scFv |
HPAB-2105-FY-S(P) | Human Anti-E2 Recombinant Antibody (clone D12); scFv Fragment | ELISA | Human scFv |
CAT | Product Name | Application | Type |
---|---|---|---|
PFBL-119 | Recombinant Human Anti-HCV E2 Antibody Fab Fragment (HC33.1) | Neut, FuncS | Fab |
PFBL-120 | Recombinant Human Anti-HCV E2 Antibody Fab Fragment (HC84-1) | WB, ELISA, Neut, FuncS | Fab |
PSBZ-180 | Recombinant Mouse Anti-HCV E2 Antibody scFv Fragment (mAb#8) | Neut | scFv |
PSBZ-181 | Recombinant Human Anti-HCV E2 Antibody scFv Fragment (hu5B3.v3) | ELISA, Neut | scFv |
PSBC-184 | Recombinant Chimeric (Human/Mouse) Anti-HCV glycoprotein E2 Antibody scFv Fragment (mAb1:7) | Neut | scFv |
CAT | Product Name | Application | Type |
---|---|---|---|
PNBL-019 | Recombinant Anti-HCV E2 VHH Single Domain Antibody (D03) | Inhib, FuncS | Llama VHH |
CAT | Product Name | Application | Type |
---|---|---|---|
TAB-020CT | Human Anti-HCV E2 Recombinant Antibody (AP33) | ELISA, IP, Neut, FC, WB | Human antibody |
TAB-238CT-S(P) | Anti-HCV E2 Recombinant Antibody scFv Fragment (Y47F) | ELISA, WB | Human antibody |
TAB-239CT-S(P) | Anti-HCV E2 Recombinant Antibody scFv Fragment (Y47W) | ELISA, WB | Human antibody |
TAB-238CT-F(E) | Anti-HCV E2 Recombinant Antibody Fab Fragment (Y47F) | ELISA, WB | Human antibody |
TAB-239CT-F(E) | Anti-HCV E2 Recombinant Antibody Fab Fragment (Y47W) | ELISA, WB | Human antibody |
CAT | Product Name | Application | Type |
---|---|---|---|
MHC-YF094 | DRB1*03:01/HPV E2 (PIVQLQGDSNCLKCFR) MHC Monomer | MHC Multimer | |
MHC-YF095 | DRB1*03:01/HPV E2 (MEAIAKRLDACQDQLLELYE) MHC Monomer | MHC Multimer | |
MHC-YF889 | DRB1*03:01/Human E2 (PIVQLQGDSNCLKCFR) MHC Tetramer | FCM | |
MHC-YF1028 | APC-DRB1*03:01/Human E2 (MEAIAKRLDACQDQLLELYE) MHC Tetramer | FCM | |
MHC-YF1041 | APC-DRB1*03:01/Human E2 (PIVQLQGDSNCLKCFR) MHC Tetramer | FCM |
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For research use only. Not intended for any clinical use. No products from Creative Biolabs may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative Biolabs.
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